Titanium alloys exhibit excellent biocompatibility and corrosion resistance in the body fluid and possess favourable mechanical properties. In order to control the tissue-implant interface and to favor cell-adhesion onto titanium, our work deals with the grafting of cell-binding peptides containing the Arginine-Glycine-Aspartic acid (RGD) sequence

Whereas the influence of the peptide sequence is well studied, there are very few studies on the role of peptide clustering. Besides, numerous works give very different values of peptide density necessary for focal contacts formation.

In the present study, we focus on the elaboration of patterned biomaterial surfaces with highly functionalized nanodomains. The grafting of an aminosilane linker on a cleaned titanium surface was then undertaken. Each of the free amino moieties was used as an initiator core for either a dendrimer synthesis, an hyperbranched polymer synthesis or the attachment of functionalized nanoparticules, therefore multiplying the number of free groups available for RGD immobilization on the material surface.

The density of grafted molecules can be quantified by XPS (X-Ray Photoelectron Spectroscopy), Scanning electron micrograph, High Resolution β-Imager or by chemical ways.

Eventually, the free functionnal sites will be used to covalently link a peptide sequence mediating cell attachment.

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